Disease relevance of Crip1

• We show that the resulting packaging cell lines psi CRIP and psi CRE can be used to isolate clones that stably produce high titers (10(6) colony-forming units/ml) of recombinant retroviruses with amphotropic and ecotropic host ranges, respectively [1].
• To study the functional activity of this family of predicted cysteine-rich proteins, the VHv1.1 gene product was produced from bacterial and baculovirus expression systems [2].
• The Sendai virus V protein is a nonstructural trans-frame protein whose cysteine-rich C-terminal half is fused to the acidic N-terminal half of the P protein via mRNA editing [3].
• Genetic analysis of determinants for spike glycoprotein assembly into murine coronavirus virions: distinct roles for charge-rich and cysteine-rich regions of the endodomain [4].
• We have found that the cysteine-rich, carboxyl-terminal region of the MSP-1 protein from the rodent malarial parasite Plasmodium yoelii yoelii can be expressed in a native configuration as a fusion protein in Escherichia coli [5].

High impact information on Crip1

• Metallothioneins (MTs), small cysteine-rich proteins, bind to and are inducible by heavy metals such as zinc, cadmium and copper [6].
• We used gene targeting to selectively disrupt cysteine-rich domain-(CRD-) containing NRG-1 isoforms [7].
• Sequence analysis of the cDNA clone revealed that the Ly-6E.1 protein consists of a 26-amino acid leader followed by a 108-residue, cysteine-rich, core protein with no N-linked glycosylation sites [8].
• We have localized an origin of replication in MEL cells to a 3-kb segment located between the 3' Igh regulatory region and Crip [9].
• The deduced amino acid sequence of the cDNA revealed a cysteine-rich protein [10].

Chemical compound and disease context of Crip1

• Improvement of recombinant retrovirus production by two psi CRIP producer cells was tested by using dexamethasone, TPA and sodium butyrate (Na-But) alone or in combination [11].

Biological context of Crip1

• During our human heart cDNA sequencing project, we have obtained a novel cDNA clone which is very similar in DNA and amino acid sequences to a rat/mouse cysteine-rich intestinal protein (1) [12].
• These properties of the psi CRIP and psi CRE packaging lines make them particularly valuable reagents for in vivo gene transfer studies aimed at cell lineage analysis and the development of human gene replacement therapies [1].
• The cysteine-rich domain protein KCP is a suppressor of transforming growth factor beta/activin signaling in renal epithelia [13].
• Protein kinase C (PKC) is an important signal transduction protein that has been proposed to interact with general anesthetics at its cysteine-rich diacylglycerol/phorbol ester-binding domain C1, a tandem repeat of C1A and C1B subdomains [14].
• Protein kinase C (PKC)-related cDNA clones isolated from mouse epidermis cDNA library encoded a 78-kDa protein, nPKC eta. nPKC eta contains a characteristic cysteine-rich repeat sequence (C1 region) and a protein kinase domain sequence (C3 region), both of which are conserved among PKC family members [15].

Anatomical context of Crip1

• A novel gene family coding for cationic, cysteine-rich peptides. Regulation in mouse small intestine and cells of myeloid origin [16].
• Consistent with this hypothesis, alteration of CRP-1 expression affected the apical trafficking of CHE-14 in vulval and rectal epithelial cells and sphingolipids (C(6)-NBD-ceramide) uptake and/or trafficking in intestinal cells [17].
• BACKGROUND: Resistin-like molecule (RELM) beta is a cysteine-rich cytokine expressed in the gastrointestinal tract and implicated in insulin resistance and gastrointestinal nematode immunity; however, its function primarily remains an enigma [18].
• To further our understanding of smooth muscle gene regulation, we characterized the cis-regulatory elements of the murine cysteine-rich protein 1 gene (CRP1/Csrp1) [19].
• Protegrin-1 (PG-1) is a cysteine-rich, 18-residue beta-sheet peptide isolated from porcine leukocytes with antimicrobial activity against a broad range of microorganisms [20].

Associations of Crip1 with chemical compounds

• These results confirm the identification of the CR region of the mannose receptor as a lectin [21].
• Reduction of the cysteine-rich defensins enhanced their ability to serve as ADP-ribose acceptors [22].
• The Raf-CRD is located in the NH2-terminal negative regulatory domain of Raf-1 and is highly homologous to cysteine-rich domains found in protein kinase C family members [23].
• Recently, a cysteine-rich gene family encoding a motif composed of invariable cysteine residues flanking hypervariable intercysteine amino acids was described (S.D. Dib-Hajj, B.A. Webb, and M.D. Summers, Proc. Natl. Acad. Sci. USA 90:3765-3769, 1993) [2].
• CRIP transgenic (Tg) mice and nontransgenic controls were challenged with lipopolysaccharide (LPS) [24].

Other interactions of Crip1

• Calreticulin (mobilferrin), cysteine-rich intestinal protein, and H(+)-adenosinetriphosphatase mRNA levels were virtually unchanged in all models [25].

Analytical, diagnostic and therapeutic context of Crip1

• The immunizations consisted of different combinations of three CIDR1 encoded by DNA followed by recombinant protein boost [26].
• Analysis of the recombinant proteins by far-UV circular dichroism suggested that the secondary structures of the autonomously expressed metalloprotease domain and the disintegrin/cysteine-rich/EGF-like domains differ from the structures present in the intact extracellular domain [27].
• Oligonucleotide primers matching the region encoding the carboxyl cysteine-rich domain of the EBA-175 were used in a polymerase chain reaction to identify homologous genes in P. berghei and P. yoelii yoelii, leading to the isolation of a P. berghei partial genomic clone [28].
• Antisera prepared against the carboxyl cysteine-rich domain of the rodent malaria EBP homologues reacted with a 120 and 128 kDa protein doublet on Western blots of P. berghei parasite antigen and showed an apical localization pattern within merozoites by indirect immunofluorescence assays [28].

References